ReviewCold Spring Harbor perspectives in medicine2013
Cystic fibrosis transmembrane conductance regulator (ABCC7) structure.
Review in Cold Spring Harbor perspectives in medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Selective amino acid formulation enhances anion secretion and restores function in cystic fibrosis mutations.Frontiers in pharmacology · 2025Article
- The molecular evolution of function in the CFTR chloride channel.The Journal of general physiology · 2021Article
- Defects in Protein Folding and/or Quality Control Cause Protein Aggregation in the Endoplasmic Reticulum.Progress in molecular and subcellular biology · 2021Article
- Mass spectrometry-based abundance atlas of ABC transporters in human liver, gut, kidney, brain and skin.FEBS letters · 2020Article
- Review
- Ligand binding to a remote site thermodynamically corrects the F508del mutation in the human cystic fibrosis transmembrane conductance regulator.The Journal of biological chemistry · 2018Article
- Structure-guided combination therapy to potently improve the function of mutant CFTRs.Nature medicine · 2018Article
- Substitution of Yor1p NBD1 residues improves the thermal stability of Human Cystic Fibrosis Transmembrane Conductance Regulator.Protein engineering, design & selection : PEDS · 2017Article
- Two Small Molecules Restore Stability to a Subpopulation of the Cystic Fibrosis Transmembrane Conductance Regulator with the Predominant Disease-causing Mutation.The Journal of biological chemistry · 2017Article
- Specific stabilization of CFTR by phosphatidylserine.Biochimica et biophysica acta. Biomembranes · 2017Article
- Molecular modelling and molecular dynamics of CFTR.Cellular and molecular life sciences : CMLS · 2017Review
- Architecture and functional properties of the CFTR channel pore.Cellular and molecular life sciences : CMLS · 2017Review
- Cytoplasmic pathway followed by chloride ions to enter the CFTR channel pore.Cellular and molecular life sciences : CMLS · 2016Article
- Positioning of extracellular loop 1 affects pore gating of the cystic fibrosis transmembrane conductance regulator.American journal of physiology. Lung cellular and molecular physiology · 2016Article
- Binding screen for cystic fibrosis transmembrane conductance regulator correctors finds new chemical matter and yields insights into cystic fibrosis therapeutic strategy.Protein science : a publication of the Protein Society · 2016Article
- Thermal stability of purified and reconstituted CFTR in a locked open channel conformation.Protein expression and purification · 2015Article
- A stable human-cell system overexpressing cystic fibrosis transmembrane conductance regulator recombinant protein at the cell surface.Molecular biotechnology · 2015Article
- Synonymous codon usage affects the expression of wild type and F508del CFTR.Journal of molecular biology · 2015Article
- State-dependent blocker interactions with the CFTR chloride channel: implications for gating the pore.Pflugers Archiv : European journal of physiology · 2014Article
- A survey of detergents for the purification of stable, active human cystic fibrosis transmembrane conductance regulator (CFTR).Biochimica et biophysica acta · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural studies of the cystic fibrosis transmembrane conductance regulator (CFTR) are reviewed. Like many membrane proteins, full-length CFTR has proven to be difficult to express and purify, hence much of the structural data available is for the more tractable, independently expressed soluble domains. Therefore, this chapter covers structural data for individual CFTR domains in addition to the sparser data available for the full-length protein. To set the context for these studies, we will start by reviewing structural information on model proteins from the ATP-binding cassette (ABC) transporter superfamily, to which CFTR belongs.
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